Baldwin S A, Perham R N, Stribling D
Biochem J. 1978 Mar 1;169(3):633-41. doi: 10.1042/bj1690633.
A new form of the class-II D-fructose 1,6-bisphosphate aldolase (EC 4.1.2.13) of Escherichia coli (Crookes' strain) was isolated from an extract of glycerol-grown bacteria. It has a higher molecular weight (approx. 80000)than previous preparations of the enzyme and closely resembles the typical class-II aldolase from yeast in size and amino acid composition. On the other hand, its kinetic behaviour is not typical of a class-II aldolase. The enzyme has no requirement for thiol compounds either for stability or activity, added K+ ions have no effect, and the optimum pH for the cleavage activity is unusually high. The class-II enzymes from the prokaryote E. coli and the eukaryote yeast show no immunological identity. However, the similarity of their structures suggests that they have evolved from a common ancestor.
从甘油培养的大肠杆菌（克鲁克斯菌株）提取物中分离出了一种新形式的II类1,6-二磷酸-D-果糖醛缩酶（EC 4.1.2.13）。它的分子量（约80000）比该酶以前的制剂更高，在大小和氨基酸组成上与酵母典型的II类醛缩酶极为相似。另一方面，其动力学行为并非II类醛缩酶的典型特征。该酶无论是稳定性还是活性都不需要硫醇化合物，添加的钾离子也没有影响，且裂解活性的最适pH异常高。原核生物大肠杆菌和真核生物酵母的II类酶没有免疫同一性。然而，它们结构的相似性表明它们是由一个共同的祖先进化而来的。
